+
Open data
-
Basic information
Entry | ![]() | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | Voltage gated potassium ion channel Kv1.2 in Sodium | |||||||||
![]() | ||||||||||
![]() |
| |||||||||
![]() | Ion Channel / Sodium bound / MEMBRANE PROTEIN | |||||||||
Function / homology | ![]() optic nerve structural organization / Voltage gated Potassium channels / voltage-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential / potassium channel complex / potassium ion export across plasma membrane / paranodal junction / regulation of circadian sleep/wake cycle, non-REM sleep / axon initial segment / corpus callosum development / voltage-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential ...optic nerve structural organization / Voltage gated Potassium channels / voltage-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential / potassium channel complex / potassium ion export across plasma membrane / paranodal junction / regulation of circadian sleep/wake cycle, non-REM sleep / axon initial segment / corpus callosum development / voltage-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential / juxtaparanode region of axon / delayed rectifier potassium channel activity / outward rectifier potassium channel activity / optic nerve development / neuronal cell body membrane / regulation of dopamine secretion / voltage-gated potassium channel activity / kinesin binding / calyx of Held / lamellipodium membrane / neuronal action potential / axon terminus / potassium ion transmembrane transport / voltage-gated potassium channel complex / sensory perception of pain / protein homooligomerization / cerebral cortex development / lamellipodium / presynaptic membrane / postsynaptic membrane / perikaryon / endosome / axon / glutamatergic synapse / dendrite / endoplasmic reticulum membrane / plasma membrane Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.17 Å | |||||||||
![]() | Wu Y / Sigworth FJ | |||||||||
Funding support | ![]()
| |||||||||
![]() | ![]() Title: Cryo-EM structures of Kv1.2 potassium channels, conducting and non-conducting. Authors: Yangyu Wu / Yangyang Yan / Youshan Yang / Shumin Bian / Alberto Rivetta / Ken Allen / Fred J Sigworth / ![]() Abstract: We present near-atomic-resolution cryo-EM structures of the mammalian voltage-gated potassium channel Kv1.2 in open, C-type inactivated, toxin-blocked and sodium-bound states at 3.2 Å, 2.5 Å, 3.2 ...We present near-atomic-resolution cryo-EM structures of the mammalian voltage-gated potassium channel Kv1.2 in open, C-type inactivated, toxin-blocked and sodium-bound states at 3.2 Å, 2.5 Å, 3.2 Å, and 2.9Å. These structures, all obtained at nominally zero membrane potential in detergent micelles, reveal distinct ion-occupancy patterns in the selectivity filter. The first two structures are very similar to those reported in the related Shaker channel and the much-studied Kv1.2-2.1 chimeric channel. On the other hand, two new structures show unexpected patterns of ion occupancy. First, the toxin α-Dendrotoxin, like Charybdotoxin, is seen to attach to the negatively-charged channel outer mouth, and a lysine residue penetrates into the selectivity filter, with the terminal amine coordinated by carbonyls, partially disrupting the outermost ion-binding site. In the remainder of the filter two densities of bound ions are observed, rather than three as observed with other toxin-blocked Kv channels. Second, a structure of Kv1.2 in Na solution does not show collapse or destabilization of the selectivity filter, but instead shows an intact selectivity filter with ion density in each binding site. We also attempted to image the C-type inactivated Kv1.2 W366F channel in Na solution, but the protein conformation was seen to be highly variable and only a low-resolution structure could be obtained. These findings present new insights into the stability of the selectivity filter and the mechanism of toxin block of this intensively studied, voltage-gated potassium channel. | |||||||||
History |
|
-
Structure visualization
-
Downloads & links
-EMDB archive
Map data | ![]() | |||
---|---|---|---|---|
Header (meta data) | ![]() | |||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 785.3 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 784.8 KB | Display | |
Data in XML | ![]() | 16.2 KB | Display | |
Data in CIF | ![]() | 20.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8vc4MC ![]() 43131 ![]() 43134 ![]() 43136 ![]() 8vc3C ![]() 8vc6C ![]() 8vchC M: atomic model generated by this map C: citing same article ( |
---|---|
Similar structure data | Similarity search - Function & homology ![]() |
-
Links
EMDB pages | ![]() ![]() |
---|---|
Related items in Molecule of the Month |
-
Map
File | ![]() | ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Voxel size | X=Y=Z: 1.068 Å | ||||||||||||||||||||
Density |
| ||||||||||||||||||||
Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
|
-Supplemental data
-
Sample components
-Entire : Voltage gated potassium channel Kv1.2 in Sodium
Entire | Name: Voltage gated potassium channel Kv1.2 in Sodium |
---|---|
Components |
|
-Supramolecule #1: Voltage gated potassium channel Kv1.2 in Sodium
Supramolecule | Name: Voltage gated potassium channel Kv1.2 in Sodium / type: cell / ID: 1 / Parent: 0 / Macromolecule list: all |
---|---|
Source (natural) | Organism: ![]() ![]() |
-Macromolecule #1: Potassium voltage-gated channel subfamily A member 2
Macromolecule | Name: Potassium voltage-gated channel subfamily A member 2 / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO |
---|---|
Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 60.59157 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MSAWSHPQFE KGGGSGGGSG GSAWSHPQFE KLVPRGSMTV ATGDPVDEAA AHPGHPQDTY DPEADHECCE RVVINISGLR FETQLKTLA QFPETLLGDP KKRMRYFDPL RNEYFFDRNR PSFDAILYYY QSGGRLRRPV NVPLDIFSEE IRFYELGEEA M EMFREDEG ...String: MSAWSHPQFE KGGGSGGGSG GSAWSHPQFE KLVPRGSMTV ATGDPVDEAA AHPGHPQDTY DPEADHECCE RVVINISGLR FETQLKTLA QFPETLLGDP KKRMRYFDPL RNEYFFDRNR PSFDAILYYY QSGGRLRRPV NVPLDIFSEE IRFYELGEEA M EMFREDEG YIKEEERPLP ENEFQRQVWL LFEYPESSGP ARIIAIVSVM VILISIVSFC LETLPIFRDE NEDMHGSGVT FH TYSQSTI GYQQSTSFTD PFFIVETLCI IWFSFEFLVR FFACPSKAGF FTNIMNIIDI VAIIPYFITL GTELAEKPED AQQ GQQAMS LAILRVIRLV RVFRIFKLSR HSKGLQILGQ TLKASMRELG LLIFFLFIGV ILFSSAVYFA EADERDSQFP SIPD AFWWA VVSMTTVGYG DMVPTTIGGK IVGSLCAIAG VLTIALPVPV IVSNFNYFYH RETEGEEQAQ YLQVTSCPKI PSSPD LKKS RSASTISKSD YMEIQEGVNN SNEDFREENL KTANCTLANT NYVNITKMLT DV UniProtKB: Potassium voltage-gated channel subfamily A member 2 |
-Experimental details
-Structure determination
Method | cryo EM |
---|---|
![]() | single particle reconstruction |
Aggregation state | particle |
-
Sample preparation
Concentration | 0.1 mg/mL |
---|---|
Buffer | pH: 7.4 |
Vitrification | Cryogen name: ETHANE |
-
Electron microscopy
Microscope | FEI TITAN KRIOS |
---|---|
Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.0 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
-
Image processing
Startup model | Type of model: NONE |
---|---|
Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.17 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 336318 |
Initial angle assignment | Type: ANGULAR RECONSTITUTION |
Final angle assignment | Type: ANGULAR RECONSTITUTION |